ANMK_NEIG1
ID ANMK_NEIG1 Reviewed; 367 AA.
AC Q5F6H5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270};
DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270};
GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=NGO1583;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N-
CC acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the
CC 1,6-anhydro ring, generating MurNAc-6-P. Is required for the
CC utilization of anhMurNAc either imported from the medium or derived
CC from its own cell wall murein, and thus plays a role in cell wall
CC recycling. {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) +
CC N-acetyl-D-muramate 6-phosphate; Xref=Rhea:RHEA:24952,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58690, ChEBI:CHEBI:58722, ChEBI:CHEBI:456216;
CC EC=2.7.1.170; Evidence={ECO:0000255|HAMAP-Rule:MF_01270};
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation. {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW90212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004969; AAW90212.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003697460.1; NC_002946.2.
DR AlphaFoldDB; Q5F6H5; -.
DR SMR; Q5F6H5; -.
DR STRING; 242231.NGO_1583; -.
DR EnsemblBacteria; AAW90212; AAW90212; NGO_1583.
DR KEGG; ngo:NGO_1583; -.
DR HOGENOM; CLU_038782_0_0_4; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006040; P:amino sugar metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR30605; PTHR30605; 1.
DR Pfam; PF03702; AnmK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250013"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ SEQUENCE 367 AA; 39995 MW; 54D01140A93219BD CRC64;
MMETQLYIGI MSGTSMDGAD AVLVRMDGGK WLGAEGHAFT PYPDRLRRKL LDLQDTGTDE
LHRSRMLSQE LSRLYAQTAA ELLCSQNLAP CDITALGCHG QTVRHAPEHG YSIQLADLPL
LAELTRIFTV GDFRSRDLAA GGQGAPLVPA FHEALFRDDR ETRVVLNIGG IANISVLPPG
APAFGFDTGP GNMLMDAWTQ AHWQLPYDKN GAKAAQGNIL PQLLGRLLAH PYFSQPHPKS
TGRELFALNW LETYLDGGEN RYDVLRTLSR FTAQTVCDAV SHAAADARQM YICGGGIRNP
VLMADLAECF GTRVSLHSTA ELNLDPQWVE AAAFAWLAAC WINRIPGSPH KATGASKPCI
LGAGYYY